Covalent structure of collagen

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Abstract
Bovine articular type II collagen was prepared by limited pepsin digestion, differential salt fractionation and carboxymethylcellulose chromatography. Cyanogen bromide digestion of purified type II collagen .alpha. chains yielded twelve distinct peptides designated CB1-12. The peptide .alpha.1(II)-CB11 was isolated by carboxymethylcellulose chromatography and Sephadex G-75S gel filtration. Automated Edman degradation together with chymotrypsin, thermolysin and trypsin digestion enabled identification of its complete amino acid sequence. Compared with type I and type III collagen, the data show similarity with .alpha.1(I)-CB8 and .alpha.1(III)-CB6-18-10-2 peptides, respectively. The peptide is located within residues 124-402 of the .alpha.1(II) collagen chain and with its identification, now extends the known amino acid sequence of bovine type II cartilage collagen to 660 amino acid residues including .alpha.(II)-CB1-2-6-12-11-8-10 (partial). This corresponds to .alpha.1(I)-CB0-1-2-4-5-8-3-7 (partial; 1-660) and .alpha.(III)-CB3A-3B-3C-7602-8-10-2-4-5 (partial; 1-660) of bovine .alpha.1(I) and .alpha.1(III) collagen chains.